I efd,griu -nl-cgeyiXY is nicteahylcl dnredeisoc a y“prrima omina daci scutruret fo a rniope”t insec het iniifonted fo a riramyP cstrtueur fo a eiptorn si “a ianelr hncai of amino ais.d”c fI you sems itwh eht imyraPr ursrcteut, as in the tensuqoi t,ems oyu ctonan fomr eht Sdorancey tercusrtu fo hte ie,potrn hicwh is temenirdde yb the don-bigdynhrgoen hchwi ccsoru ntbweee het petedip bekabcno, denndepetni of the R psgro.u I peoh tish daem ess.ne
mrFo wiipdekia: eo“cSydnra suretcurt is armlfylo eenddfi yb hte atterpn fo dynroehg sbdon entbewe eth noaim gdoernyh dan rxclyoab gxyeon mtsao ni hte epetipd acnoebkb.” hesapmsi( me)in
From Molecular Biology of the Cell:
Biologists distinguish four levels of organization in the structure of a protein. The amino acid sequence is known as the primary structure of the protein. Stretches of polypeptide chain that form α helices and β sheets constitute the protein’s secondary structure. The full three-dimensional organization of a polypeptide chain is sometimes referred to as the protein’s tertiary structure, and if a particular protein molecule is formed as a complex of more than one polypeptide chain, the complete structure is designated as the quaternary structure.
ok ugys adn i uoqet omfr losuhw0:ert2tt.lpbfpg.aetespo/o/soc/cecssteiar/modtwre-4ii/s1wimhnet
%90" haev na iiatidelebfn cnietge nimoautt
CLO 11A dan OLC 1A2
c
asesu anabomlr ncaoglle nrioinclks-gs avi a gcleyni tostbiuuistn in het rcongleopla emcllueo "
hwhci emsan ttha OI ash a cyeilgn tituiobntsus nda efherrto tis elbnau ot mofr a nasdrcoey cesuturu.tr
uDe to cysenlg'i sllam ei,sz ti eecsrat "k"nsik in hte inaom cida enqeceu.s eshTe snkki ear dedeen ot ecorryltc rofm eth soyndacre turru.etsc
tOher esw:nsar
Gy-lYX- is bconekba ofr glneloca haapl ina.hc 3 engcloal alpha inchas pisalr to fmor irtepl x.elhi eniGlyc ahs on R ,ogrup gnalwiol for lexifbyltii and tmfnrooai of lrtipe .hilex oN cglyine venspret isth uionsntcou ri,sgnlaip einerpntgv hte rmtiafnoo fo eolcgaln aocrsnyed trtecusru.
eacllR tath -ahchsileplae and etshbsetea- rea salemepx of rdcaoseny sr.eurtscut hTis can eb ohhtgtu fo a tmoafisnteina fo het phala xhli.e
torAeNh ywa to get ta it is iav inlano:mieit
A. ondrgehy donibng wndtoul llryea hgcaen cisne ehetnri lianaen nor cglnyie rea .r pBoal lGy g;&t Ala 'nhltdosu agnche how poienrl is ifddeiom I( aenm ti OCDUL, if rhete wsa a sterci cinenhrad or ,segotmnih tub not a terga n)Dr s.wea ghinont ot indactei hatt cnlalgoe eaddirognet is etlrdea in osnepres ot na AA ts.sbntitiouu A,los ni het xeotnct fo OI hwic(h is het rnipteesng )mlcnop,ati we aerdaly knwo ahtt het eobrmlp ndots'e have ynitaghn ot od with tion,daegerd moer hwti eht hgcaen in tresfru.tunEcoutin c/ nytesoHl t'odn .kwno
eHser’ oen ywa to opelsiefat--monercis acerdsee“d rdhygnoebo-dn am:”tfonoir ’Im nto a big fan of hsit lnie of ero,ginans btu lceaytinlch lnieaan as a esdi pugro sah eorm hregds*oyn fro otpnteial ghornyed bnnogid atnh lnyigec:
einaal:n 3HC—
nicelyg: —H
o,S i,“claylhncte” anainel wluod rteimp rome bgo-hdnoydern ifarnoo,tm chhwi mhitg lowal yuo ot lmaeineit htat h.oicec
Ttah ds,ai ti esems lstmao siboilmsep to leur out uiotthw( ryve nccathlie eglwonked ro soem ddrpvioe ratnpliemeex adta) atht teh lyilthgs raglre lanaeni sdeo ont rmpaii endyrgoh innodbg enewteb eolngacl melosulce aiv rtscie (aa)pistl efitcrene.ner nI pleirsm se,rmt nscie naaleni si grla,er uyo ulowd thkni htat it tums hmeosow iernfteer whti the ro-ngiobhddngnye that sccuro iwth eht twdyie-lp eylcngi.
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Syrctitl* npgsika,e ’ist not teh emnrbu fo rnhdgseyo btu laos het nhrstget fo hte iolped atth fsieltcitaa ygrnoehd bi:gdnon a rynoehgd dnbou ot a lrsngyto raetclvnteoeeig elucmeol elki ruflnoie lilw apap“”re eomr septvioi an,d tsu,h h-nognryodedb remo ryostgnl thiw a eraybn xygnoe (mocaperd ihtw a rneghoyd ecdnnotce to ,abonrc rof ael.)pemx
ertFurh e:arngdi
From Molecular Biology of the Cell:
Hydroxylysines and hydroxyprolines are infrequently found in other animal proteins, although hydroxyproline is abundant in some proteins in the plant cell wall. In collagen, the hydroxyl groups of these amino acids are thought to form interchain hydrogen bonds that help stabilize the triple-stranded helix. Conditions that prevent proline hydroxylation, such as a deficiency of ascorbic acid (vitamin C), have serious consequences. (Emphasis mine)
From Molecular Biology of the Cell:
The primary feature of a typical collagen molecule is its long, stiff, triple-stranded helical structure, in which three collagen polypeptide chains, called α chains, are wound around one another in a ropelike superhelix (Figure 19-43). Collagens are extremely rich in proline and glycine, both of which are important in the formation of the triple-stranded helix. Proline, because of its ring structure, stabilizes the helical conformation in each α chain, while glycine is regularly spaced at every third residue throughout the central region of the α chain. Being the smallest amino acid (having only a hydrogen atom as a side chain), glycine allows the three helical α chains to pack tightly together to form the final collagen superhelix (see Figure 19-43).
I tihmg eb gienokivhnrt it ub,t H bndo nmrioatof of s'aa meksa eht yocardnse cruetutrs fo teh tronpie (ocleanlg ni this sc.a)e eTh lyG ot Aal iuitubnsstto sode lersut ni elss H dbno rfmitno,ao utb fo nilivddaui 'saa tno wteeneb cngoeall secoemllu (hatt mghti eb orem orf uqaaeyrntr tuctesrru)
airrPmy ruestrutc = inmoa dcia cecornySseeua ndeq rcursetut = uutsrecrt ofdrem iwht a geisln moian diac euceneqs (btea adptele hest,e laaph xehil, ttyarricT)ee ctsreuutr = uitleplm ydcsornea usucrettsr ieancgtnirt rttheoeg pim(tllue tbae ldeepat ethsse tsacked on top fo ahce hrtoe, reyatu)rnceart Q ecurtutrs = priotne srructteu medofr from loidfng of all eratriyt etsursuctr to aekm biingdn t,ssie te.c
cnSie eht ineaanl saw ptu in pcael of het ic,eyGnl hte ryrampi rutrsetcu wsa elaunb ot fmro an alpha ilxeh nsiec lahpa eixhl tucresurts eend a tuiaprlcra nceueqes y(lg - x- y) in roedr ot ofrm ngoehyrd snodb to epke teh xlihe tbs.ela
tawh is llcagoen ? a rndoasyce noipter rutctes.ru
henw oyu reemvo leicyn,g teh otsm dnnuaabt amion cdia , mfro het rrspoceur ecloulem wlil you etg a oerrpp onyresacd tetusrruc ? NO
yGl si r,pola Aelnnai is nornolap dna yhopbd.rohic nsseeMsi tonianecensrvvo muoa.ntit ehesT AsA avhe rifdenetf lhecmcai eeporsptir ichhw lade to sdtpuidre itronpe ifdglon sadren(ocy trs)ecutur. rimaSil to lGu - Val ttubiniutsso in ikScel Clle i.eseaDs
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